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1 This topic review contains data on the enzymatic and antioxidant properties of serum albumin; the prospects for the therapeutic application of the functional features of the protein are discussed. Nikolay Goncharov + 2106 word(s) 2106 2020-10-12 05:49:58 |
2 Format correct Vicky Zhou + 1929 word(s) 4035 2020-12-31 05:09:09 | |
3 format correct Catherine Yang -3015 word(s) 1020 2022-04-13 10:32:38 | |
4 format correct Catherine Yang -6 word(s) 1014 2022-04-13 10:33:29 |

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Belinskaia, D.A.; Voronina, P.A.; Shmurak, V.I.; Vovk, M.A.; Batalova, A.A.; Jenkins, R.O.; Goncharov, N.V.; Belinskaia, D. Serum Albumin. Encyclopedia. Available online: https://encyclopedia.pub/entry/2844 (accessed on 21 September 2026).
Belinskaia DA, Voronina PA, Shmurak VI, Vovk MA, Batalova AA, Jenkins RO, et al. Serum Albumin. Encyclopedia. Available at: https://encyclopedia.pub/entry/2844. Accessed September 21, 2026.
Belinskaia, Daria A., Polina A. Voronina, Vladimir I. Shmurak, Mikhail A. Vovk, Anastasia A. Batalova, Richard O. Jenkins, Nikolay V. Goncharov, Daria Belinskaia. "Serum Albumin" Encyclopedia, https://encyclopedia.pub/entry/2844 (accessed September 21, 2026).
Belinskaia, D.A., Voronina, P.A., Shmurak, V.I., Vovk, M.A., Batalova, A.A., Jenkins, R.O., Goncharov, N.V., & Belinskaia, D. (2020, October 30). Serum Albumin. In Encyclopedia. https://encyclopedia.pub/entry/2844
Belinskaia, Daria A., et al. "Serum Albumin." Encyclopedia. Web. 30 October, 2020.
Peer Reviewed
Serum Albumin
This is a peer-reviewed entry published in Encyclopedia Journal, full entry can be found at 10.3390/encyclopedia1010009

Being one of the most abundant proteins in human and other mammals, albumin plays a crucial role in transporting various endogenous and exogenous molecules and maintaining of colloid osmotic pressure of the blood. It is not only the passive but also the active participant of the pharmacokinetic and toxicokinetic processes possessing a number of enzymatic activities. A free thiol group of the albumin molecule determines the participation of the protein in redox reactions. Its activity is not limited to interaction with other molecules entering the blood: of great physiological importance is its interaction with the cells of blood, blood vessels and also outside the vascular bed. This topic review contains data on the enzymatic, inflammatory and antioxidant properties of serum albumin. 

albumin blood plasma enzymatic activities oxidative stress

References

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  2. Haefliger, D.N.; Moskaitis, J.E.; Schoenberg, D.R.; Wahli, W. Amphibian albumins as members of the albumin, alpha-fetoprotein, vitamin D-binding protein multigene family. J. Mol. Evol. 1989, 29, 344–354.
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  6. Albumin. Available online: http://albumin.org/ (accessed on 22 December 2020).
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  9. Lu, R.; Li, W.W.; Katzir, A.; Raichlin, Y.; Yu, H.Q.; Mizaikoff, B. Probing the secondary structure of bovine serum albumin during heat-induced denaturation using mid-infrared fiberoptic sensors. Analyst 2015, 140, 765–770.
  10. He, X.M.; Carter, D.C. Atomic structure and chemistry of human serum albumin. Nature 1992, 358, 209–215.
  11. Bujacz, A. Structures of bovine, equine and leporine serum albumin. Acta Crystallogr. D Biol. Crystallogr. 2012, 68, 1278–1289.
  12. Hein, K.L.; Kragh-Hansen, U.; Morth, J.P.; Jeppesen, M.D.; Otzen, D.; Møller, J.V.; Nissen, P. Crystallographic analysis reveals a unique lidocaine binding site on human serum albumin. J. Struct. Biol. 2010, 171, 353–360.
  13. Kragh-Hansen, U.; Brennan, S.O.; Galliano, M.; Sugita, O. Binding of warfarin, salicylate, and diazepam to genetic variants of human serum albumin with known mutations. Mol. Pharmacol. 1990, 37, 238–242.
  14. Fasano, M.; Curry, S.; Terreno, E.; Galliano, M.; Fanali, G.; Narciso, P.; Notari, S.; Ascenzi, P. The extraordinary ligand binding properties of human serum albumin. IUBMB Life 2005, 57, 787–796.
  15. Ascenzi, P.; Bocedi, A.; Notari, S.; Fanali, G.; Fesce, R.; Fasano, M. Allosteric modulation of drug binding to human serum albumin. Mini Rev. Med. Chem. 2006, 6, 483–489.
  16. Ascenzi, P.; Fasano, M. Allostery in a monomeric protein: The case of human serum albumin. Biophys. Chem. 2010, 148, 16–22.
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Subjects: Biochemistry & Molecular Biology
Contributors MDPI registered users' name will be linked to their SciProfiles pages. To register with us, please refer to https://encyclopedia.pub/register : Daria A. Belinskaia ,
Polina A. Voronina
,
Vladimir I. Shmurak
, Mikhail A. Vovk ,
Anastasia A. Batalova
, Richard O. Jenkins , Nikolay V. Goncharov , Daria Belinskaia
View Times: 6.3K
Online Date: 30 Oct 2020
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